Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-asparaginase 1

Gene

ASP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641O-isoaspartyl threonine intermediatePROSITE-ProRule annotation
Binding sitei110 – 1101SubstrateBy similarity

GO - Molecular functioni

  • asparaginase activity Source: SGD

GO - Biological processi

  • asparagine catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciYEAST:YDR321W-MONOMER.
BRENDAi3.5.1.1. 984.
SABIO-RKP38986.

Names & Taxonomyi

Protein namesi
Recommended name:
L-asparaginase 1 (EC:3.5.1.1)
Alternative name(s):
L-asparaginase I
L-asparagine amidohydrolase I
Short name:
ASP I
Gene namesi
Name:ASP1
Ordered Locus Names:YDR321W
ORF Names:D9798.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR321W.
SGDiS000002729. ASP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • intracellular Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761A → V: Almost no activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381L-asparaginase 1PRO_0000171091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei350 – 3501PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38986.
PRIDEiP38986.

PTM databases

iPTMnetiP38986.

Expressioni

Inductioni

Expressed constitutively.

Interactioni

Subunit structurei

Homopolymer.

Protein-protein interaction databases

BioGridi32378. 19 interactions.
DIPiDIP-4030N.
IntActiP38986. 17 interactions.
MINTiMINT-497546.

Structurei

3D structure databases

ProteinModelPortaliP38986.
SMRiP38986. Positions 52-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 378325Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 1422Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the asparaginase 1 family.Curated
Contains 1 asparaginase/glutaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000050435.
HOGENOMiHOG000044165.
InParanoidiP38986.
KOiK01424.
OMAiPRYYRRP.
OrthoDBiEOG75TMN3.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38986-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSDSVEITT ICPDVENSQF VVQSNCPETI PEILKSQNAA VNGSGIACQQ
60 70 80 90 100
RSLPRIKILG TGGTIASKAI DSSQTAGYHV DLTIQDLLDA IPDISKVCDI
110 120 130 140 150
EYEQLCNVDS KDINEDILYK IYKGVSESLQ AFDGIVITHG TDTLSETAFF
160 170 180 190 200
IESTIDAGDV PIVFVGSMRP STSVSADGPM NLYQAICIAS NPKSRGRGVL
210 220 230 240 250
VSLNDQISSG YYITKTNANS LDSFNVRQGY LGNFVNNEIH YYYPPVKPQG
260 270 280 290 300
CHKFKLRVDG KHFKLPEVCI LYAHQAFPPA IVNLVADKYD GIVLATMGAG
310 320 330 340 350
SLPEEVNETC MKLSLPIVYS KRSMDGMVPI ANVPKKGSKE DNLIASGYLS
360 370 380
PEKSRILLQL CLAGNYTLEE IKHVFTGVYG G
Length:381
Mass (Da):41,395
Last modified:February 1, 1995 - v1
Checksum:i8204CB7C58B5B75F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27406 Genomic DNA. Translation: CAA81794.1.
U32517 Genomic DNA. Translation: AAB64757.1.
BK006938 Genomic DNA. Translation: DAA12163.1.
PIRiS48513.
RefSeqiNP_010607.3. NM_001180629.3.

Genome annotation databases

EnsemblFungiiYDR321W; YDR321W; YDR321W.
GeneIDi851920.
KEGGisce:YDR321W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27406 Genomic DNA. Translation: CAA81794.1.
U32517 Genomic DNA. Translation: AAB64757.1.
BK006938 Genomic DNA. Translation: DAA12163.1.
PIRiS48513.
RefSeqiNP_010607.3. NM_001180629.3.

3D structure databases

ProteinModelPortaliP38986.
SMRiP38986. Positions 52-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32378. 19 interactions.
DIPiDIP-4030N.
IntActiP38986. 17 interactions.
MINTiMINT-497546.

PTM databases

iPTMnetiP38986.

Proteomic databases

MaxQBiP38986.
PRIDEiP38986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR321W; YDR321W; YDR321W.
GeneIDi851920.
KEGGisce:YDR321W.

Organism-specific databases

EuPathDBiFungiDB:YDR321W.
SGDiS000002729. ASP1.

Phylogenomic databases

GeneTreeiENSGT00510000050435.
HOGENOMiHOG000044165.
InParanoidiP38986.
KOiK01424.
OMAiPRYYRRP.
OrthoDBiEOG75TMN3.

Enzyme and pathway databases

BioCyciYEAST:YDR321W-MONOMER.
BRENDAi3.5.1.1. 984.
SABIO-RKP38986.

Miscellaneous databases

PROiP38986.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase."
    Sinclair K., Warner J.P., Bonthron D.T.
    Gene 144:37-43(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiASPG1_YEAST
AccessioniPrimary (citable) accession number: P38986
Secondary accession number(s): D6VSV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Yeast contains two L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.